Evidence map›Paper›PMID 33166396›Full record

ArticleNucleic acids research2020

The catalytic activity of the translation termination factor methyltransferase Mtq2-Trm112 complex is required for large ribosomal subunit biogenesis.

Caroline Lacoux, Ludivine Wacheul, Kritika Saraf, Nicolas Pythoud, Emmeline Huvelle, Sabine Figaro, Marc Graille, Christine Carapito, Denis L J Lafontaine, Valérie Heurgué-Hamard

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.7field-weighted citation impact, top 32% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

10 citing papers in PubMed, 19 citations in OpenAlex.

  1. Review
  2. CytosolicProceedings of the National Academy of Sciences of the United States of America · 2024
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors at 2 institutions in 2 countries.

Caroline LacouxUMR8261 (CNRS, Université de Paris), Institut de Biologie Physico-Chimique, 13 rue Pierre et Marie Curie, 75005 Paris, France.
Ludivine WacheulRNA Molecular Biology, Fonds de la Recherche Scientifique (F.R.S.-FNRS), Université Libre de Bruxelles Cancer Research Center (U-CRC), Center for Microscopy and Molecular Imaging (CMMI), Gosselies, Belgium.
Kritika SarafRNA Molecular Biology, Fonds de la Recherche Scientifique (F.R.S.-FNRS), Université Libre de Bruxelles Cancer Research Center (U-CRC), Center for Microscopy and Molecular Imaging (CMMI), Gosselies, Belgium.
Nicolas PythoudLaboratoire de Spectrométrie de Masse Bio-Organique (LSMBO), UMR 7178, IPHC, Université de Strasbourg, CNRS, Strasbourg, France.
Emmeline HuvelleUMR8261 (CNRS, Université de Paris), Institut de Biologie Physico-Chimique, 13 rue Pierre et Marie Curie, 75005 Paris, France.
Sabine FigaroUMR8261 (CNRS, Université de Paris), Institut de Biologie Physico-Chimique, 13 rue Pierre et Marie Curie, 75005 Paris, France.
Marc GrailleLaboratoire de Biologie Structurale de la Cellule (BIOC), CNRS, Ecole polytechnique, Institut Polytechnique de Paris, F-91128 Palaiseau, France.
Christine CarapitoLaboratoire de Spectrométrie de Masse Bio-Organique (LSMBO), UMR 7178, IPHC, Université de Strasbourg, CNRS, Strasbourg, France.
Denis L J LafontaineRNA Molecular Biology, Fonds de la Recherche Scientifique (F.R.S.-FNRS), Université Libre de Bruxelles Cancer Research Center (U-CRC), Center for Microscopy and Molecular Imaging (CMMI), Gosselies, Belgium.
Valérie Heurgué-HamardUMR8261 (CNRS, Université de Paris), Institut de Biologie Physico-Chimique, 13 rue Pierre et Marie Curie, 75005 Paris, France.
Centre National de la Recherche Scientifique · FRUniversité Libre de Bruxelles · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Mtq2-Trm112 methyltransferase modifies the eukaryotic translation termination factor eRF1 on the glutamine side chain of a universally conserved GGQ motif that is essential for release of newly synthesized peptides. Although this modification is found in the three domains of life, its exact role in eukaryotes remains unknown. As the deletion of MTQ2 leads to severe growth impairment in yeast, we have investigated its role further and tested its putative involvement in ribosome biogenesis. We found that Mtq2 is associated with nuclear 60S subunit precursors, and we demonstrate that its catalytic activity is required for nucleolar release of pre-60S and for efficient production of mature 5.8S and 25S rRNAs. Thus, we identify Mtq2 as a novel ribosome assembly factor important for large ribosomal subunit formation. We propose that Mtq2-Trm112 might modify eRF1 in the nucleus as part of a quality control mechanism aimed at proof-reading the peptidyl transferase center, where it will subsequently bind during translation termination.

Indexed as

Gene Expression Regulation, FungalOrganelle BiogenesisBinding SitesBiocatalysisCloning, MolecularCrystallography, X-RayEscherichia coliGenetic VectorsMethyltransferasesModels, MolecularPeptide Chain Termination, TranslationalPeptide Termination FactorsProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein Interaction Domains and MotifsMethyltransferasesMTQ2 protein, S cerevisiaePeptide Termination FactorsRecombinant ProteinsRNA, RibosomalRNA, ribosomal, 25SRNA, Ribosomal, 5.8SSaccharomyces cerevisiae ProteinsSUP45 protein, S cerevisiaeTrm112 protein, S cerevisiaetRNA Methyltransferases

Identifiers

PMID33166396
PMCPMC7708063
OpenAlexW3100898025

What Socratic holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.